Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

Aseem Mishra; Anurag Misra; T. Sri Vaishnavi; Chaitanya Thota; Madhvi Gupta; Suryanarayanarao Ramakumar; Virander Singh Chauhan

doi:10.1039/c3cc38982k

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

Aseem Mishra
, Anurag Misra
, T. Sri Vaishnavi
, Chaitanya Thota
, Madhvi Gupta
, Suryanarayanarao Ramakumar
, Virander Singh Chauhan

Research output: Contribution to journal › Article › peer-review

49 Scopus citations

Abstract

hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.

Original language	English (US)
Pages (from-to)	2688-2690
Number of pages	3
Journal	Chemical Communications
Volume	49
Issue number	26
DOIs	https://doi.org/10.1039/c3cc38982k
State	Published - Mar 5 2013
Externally published	Yes

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Catalysis
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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abstract = "hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.",

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AU - Mishra, Aseem

AU - Misra, Anurag

AU - Sri Vaishnavi, T.

AU - Thota, Chaitanya

AU - Gupta, Madhvi

AU - Ramakumar, Suryanarayanarao

AU - Chauhan, Virander Singh

PY - 2013/3/5

Y1 - 2013/3/5

N2 - hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.

AB - hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.

UR - https://www.scopus.com/pages/publications/84874855623

UR - https://www.scopus.com/pages/publications/84874855623#tab=citedBy

U2 - 10.1039/c3cc38982k

DO - 10.1039/c3cc38982k

M3 - Article

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AN - SCOPUS:84874855623

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EP - 2690

JO - Chemical Communications

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ER -

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

Abstract

ASJC Scopus subject areas

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